Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin.
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Extensions of PSD-95/discs large/ZO-1 (PDZ) domains influence lipid binding and membrane targeting of syntenin-1Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipidsEvidence that membrane insertion of the cytosolic domain of Bcl-xL is governed by an electrostatic mechanismAdducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neuronsX MARCKS the spot: myristoylated alanine-rich C kinase substrate in neuronal function and diseaseCrystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/calmodulinPerturbation of a very late step of regulated exocytosis by a secretory carrier membrane protein (SCAMP2)-derived peptideMyristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayersIdentification and characterization of cathepsin B as the cellular MARCKS cleaving enzymeMyristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cellsAltered patterns of sucrose synthase phosphorylation and localization precede callose induction and root tip death in anoxic maize seedlingsLocation and dynamics of basic peptides at the membrane interface: electron paramagnetic resonance spectroscopy of tetramethyl-piperidine-N-oxyl-4-amino-4-carboxylic acid-labeled peptidesCharacterization of a Rac1- and RhoGDI-associated lipid kinase signaling complex.Myristoylated, alanine-rich C-kinase substrate phosphorylation regulates growth cone adhesion and pathfindingDynamic adhesions and MARCKS in melanoma cellsThe secretory carrier membrane protein family: structure and membrane topology.Location of the myristoylated alanine-rich C-kinase substrate (MARCKS) effector domain in negatively charged phospholipid bicelles.Detection of highly curved membrane surfaces using a cyclic peptide derived from synaptotagmin-I.Membrane-inserted conformation of transmembrane domain 4 of divalent-metal transporter.Phosphatidylserine liposomes can be tethered by caldesmon to actin filamentsBinding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results.Calculations of the electrostatic potential adjacent to model phospholipid bilayersElectrostatic properties of membranes containing acidic lipids and adsorbed basic peptides: theory and experimentBinding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results.Biophysical investigations with MARCKS-ED: dissecting the molecular mechanism of its curvature sensing behaviors.Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains.Cross-talk unfolded: MARCKS proteins.Molecular and cellular adaptations of maize to flooding stress.Sequestration of phosphoinositides by mutated MARCKS effector domain inhibits stimulated Ca(2+) mobilization and degranulation in mast cells.An electrostatic switch controls palmitoylation of the large conductance voltage- and calcium-activated potassium (BK) channel.Group IVA phospholipase A₂ is necessary for growth cone repulsion and collapse.MARCKS-ED peptide as a curvature and lipid sensorRaf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells.Myristoylated and non-myristoylated forms of the pH sensor protein hisactophilin II: intracellular shuttling to plasma membrane and nucleus monitored in real time by a fusion with green fluorescent protein.Myristoylated Alanine-Rich Protein Kinase Substrate (MARCKS) Regulates Small GTPase Rac1 and Cdc42 Activity and Is a Critical Mediator of Vascular Smooth Muscle Cell Migration in Intimal Hyperplasia Formation.Regulation of PI3K by PKC and MARCKS: Single-Molecule Analysis of a Reconstituted Signaling PathwayA cell cycle kinase with tandem sensory PAS domains integrates cell fate cues.Determinants of Curvature-Sensing Behavior for MARCKS-Fragment PeptidesDrugging Membrane Protein Interactions.Cellular membranes and lipid-binding domains as attractive targets for drug development.
P2860
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P2860
Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin.
description
1994 nî lūn-bûn
@nan
1994 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Phosphorylation reverses the m ...... ns of MARCKS and neuromodulin.
@ast
Phosphorylation reverses the m ...... ns of MARCKS and neuromodulin.
@en
Phosphorylation reverses the m ...... ns of MARCKS and neuromodulin.
@nl
type
label
Phosphorylation reverses the m ...... ns of MARCKS and neuromodulin.
@ast
Phosphorylation reverses the m ...... ns of MARCKS and neuromodulin.
@en
Phosphorylation reverses the m ...... ns of MARCKS and neuromodulin.
@nl
prefLabel
Phosphorylation reverses the m ...... ns of MARCKS and neuromodulin.
@ast
Phosphorylation reverses the m ...... ns of MARCKS and neuromodulin.
@en
Phosphorylation reverses the m ...... ns of MARCKS and neuromodulin.
@nl
P2093
P2860
P1433
P1476
Phosphorylation reverses the m ...... ns of MARCKS and neuromodulin.
@en
P2093
J D Johnson
P J Blackshear
S McLaughlin
P2860
P304
P356
10.1016/S0006-3495(94)80473-4
P407
P577
1994-07-01T00:00:00Z